2000 character limit reached
Non-equilibrium physics of multi-species assembly: From inhibition of fibrils in biomolecular condensates to growth of online distrust
Published 14 Dec 2023 in physics.bio-ph and physics.app-ph | (2312.08609v1)
Abstract: Self-assembly is a key process in living systems - from the microscopic biological level (e.g. assembly of proteins into fibrils within biomolecular condensates in a human cell) through to the macroscopic societal level (e.g. assembly of humans into common-interest communities across online social media platforms). The components in such systems (e.g. macromolecules, humans) are highly diverse, and so are the self-assembled structures that they form. However, there is no simple theory of how such structures assemble from a multi-species pool of components. Here we provide a very simple model which trades myriad chemical and human details for a transparent analysis, and yields results in good agreement with recent empirical data. It reveals a new inhibitory role for biomolecular condensates in the formation of dangerous amyloid fibrils, as well as a kinetic explanation of why so many diverse distrust movements are now emerging across social media. The nonlinear dependencies that we uncover suggest new real-world control strategies for such multi-species assembly.
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E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Bożyk, A., Wojas-Krawczyk, K., Krawczyk, P., Milanowski, J.: Tumor microenvironment-a short review of cellular and interaction diversity. Biology 18(929) (2022) https://doi.org/10.3390/biology11060929 Li and Barzin Y. [2019] Li, I., Barzin Y., N.: Exosomes in the tumor microenvironment as mediators of cancer therapy resistance. Molecular Cancer 18(32) (2019) https://doi.org/10.1186/s12943-019-0975-5 Hinshaw and Shevde [2019] Hinshaw, D.C., Shevde, L.A.: The Tumor Microenvironment Innately Modulates Cancer Progression. Cancer Research 79(18), 4557–4566 (2019) https://doi.org/10.1158/0008-5472.CAN-18-3962 Küffner et al. [2021] Küffner, A.M., Linsenmeier, M., Grigolato, F., Prodan, M., Zuccarini, R., Capasso Palmiero, U., Faltova, L., Arosio, P.: Sequestration within biomolecular condensates inhibits aβ𝛽\betaitalic_β-42 amyloid formation. Chem. Sci. 12, 4373–4382 (2021) https://doi.org/10.1039/D0SC04395H Lipiński et al. [2022] Lipiński, W.P., Visser, B.S., Robu, I., Fakhree, M.A.A., Lindhoud, S., Claessens, M.M.A.E., Spruijt, E.: Biomolecular condensates can both accelerate and suppress aggregation of α𝛼\alphaitalic_α-synuclein. Science Advances 8(48), 6495 (2022) https://doi.org/10.1126/sciadv.abq6495 Johnson et al. [2020] Johnson, N.F., Velásquez, N., Restrepo, N.J., Leahy, R., Gabriel, N., El Oud, S., Zheng, M., Manrique, P., Wuchty, S., Lupu, Y.: The online competition between pro-and anti-vaccination views. Nature 582(7811), 230–233 (2020) Illari et al. [2022] Illari, L., Restrepo, N.J., Johnson, N.F.: Losing the battle over best-science guidance early in a crisis: Covid-19 and beyond. Science Advances 8(39), 8017 (2022) https://doi.org/10.1126/sciadv.abo8017 Bolnick et al. [2011] Bolnick, D.I., Amarasekare, P., Araújo, M.S., Bürger, R., Levine, J.M., Novak, M., Rudolf, V.H.W., Schreiber, S.J., Urban, M.C., Vasseur, D.A.: Why intraspecific trait variation matters in community ecology. Trends in ecology & evolution 26(4), 183–192 (2011) https://doi.org/10.1016/j.tree.2011.01.009 Siefert et al. [2015] Siefert, A., Violle, C., Chalmandrier, L., Albert, C.H., Taudiere, A., Fajardo, A., Aarssen, L.W., Baraloto, C., Carlucci, M.B., Cianciaruso, M.V., L. Dantas, V., Bello, F., Duarte, L.D.S., Fonseca, C.R., Freschet, G.T., Gaucherand, S., Gross, N., Hikosaka, K., Jackson, B., Jung, V., Kamiyama, C., Katabuchi, M., Kembel, S.W., Kichenin, E., Kraft, N.J.B., Lagerström, A., Bagousse-Pinguet, Y.L., Li, Y., Mason, N., Messier, J., Nakashizuka, T., Overton, J.M., Peltzer, D.A., Pérez-Ramos, I.M., Pillar, V.D., Prentice, H.C., Richardson, S., Sasaki, T., Schamp, B.S., Schöb, C., Shipley, B., Sundqvist, M., Sykes, M.T., Vandewalle, M., Wardle, D.A.: A global meta-analysis of the relative extent of intraspecific trait variation in plant communities. Ecology Letters 18(12), 1406–1419 (2015) https://doi.org/10.1111/ele.12508 Forsythe et al. [2021] Forsythe, A.B., Day, T., Nelson, W.A.: Demystifying individual heterogeneity. Ecology Letters 24(10), 2282–2297 (2021) https://doi.org/10.1111/ele.13843 Jackson and Xue [2023] Jackson, Z., Xue, B.: Heterogeneity of interaction strengths and its consequences on ecological systems. Sci Rep 13(1905) (2023) https://doi.org/10.1038/s41598-023-28473-8 Johnson et al. [2016] Johnson, N.F., Zheng, M., Vorobyeva, Y., Gabriel, A., Qi, H., Velásquez, N., Manrique, P., Johnson, D., Restrepo, E., Song, C., et al.: New online ecology of adversarial aggregates: Isis and beyond. Science 352(6292), 1459–1463 (2016) Manrique et al. [2018] Manrique, P.D., Zheng, M., Cao, Z., Restrepo, E.M., Johnson, N.F.: Generalized gelation theory describes onset of online extremist support. Phys. Rev. Lett. 121(4), 048301 (2018) Velásquez et al. [2021] Velásquez, N., Manrique, P., Sear, R., et al.: Hidden order across online extremist movements can be disrupted by nudging collective chemistry. Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. [2023] Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. Lett. 130, 237401 (2023) https://doi.org/10.1103/PhysRevLett.130.237401 Krapivsky et al. [2010] Krapivsky, P.L., Redner, S., Ben-Naim, E.: A Kinetic View of Statistical Physics. Cambridge University Press, ??? (2010). https://doi.org/10.1017/CBO9780511780516 Newman [2018] Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. [2009] Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Li, I., Barzin Y., N.: Exosomes in the tumor microenvironment as mediators of cancer therapy resistance. Molecular Cancer 18(32) (2019) https://doi.org/10.1186/s12943-019-0975-5 Hinshaw and Shevde [2019] Hinshaw, D.C., Shevde, L.A.: The Tumor Microenvironment Innately Modulates Cancer Progression. Cancer Research 79(18), 4557–4566 (2019) https://doi.org/10.1158/0008-5472.CAN-18-3962 Küffner et al. [2021] Küffner, A.M., Linsenmeier, M., Grigolato, F., Prodan, M., Zuccarini, R., Capasso Palmiero, U., Faltova, L., Arosio, P.: Sequestration within biomolecular condensates inhibits aβ𝛽\betaitalic_β-42 amyloid formation. Chem. Sci. 12, 4373–4382 (2021) https://doi.org/10.1039/D0SC04395H Lipiński et al. [2022] Lipiński, W.P., Visser, B.S., Robu, I., Fakhree, M.A.A., Lindhoud, S., Claessens, M.M.A.E., Spruijt, E.: Biomolecular condensates can both accelerate and suppress aggregation of α𝛼\alphaitalic_α-synuclein. Science Advances 8(48), 6495 (2022) https://doi.org/10.1126/sciadv.abq6495 Johnson et al. [2020] Johnson, N.F., Velásquez, N., Restrepo, N.J., Leahy, R., Gabriel, N., El Oud, S., Zheng, M., Manrique, P., Wuchty, S., Lupu, Y.: The online competition between pro-and anti-vaccination views. Nature 582(7811), 230–233 (2020) Illari et al. [2022] Illari, L., Restrepo, N.J., Johnson, N.F.: Losing the battle over best-science guidance early in a crisis: Covid-19 and beyond. Science Advances 8(39), 8017 (2022) https://doi.org/10.1126/sciadv.abo8017 Bolnick et al. [2011] Bolnick, D.I., Amarasekare, P., Araújo, M.S., Bürger, R., Levine, J.M., Novak, M., Rudolf, V.H.W., Schreiber, S.J., Urban, M.C., Vasseur, D.A.: Why intraspecific trait variation matters in community ecology. Trends in ecology & evolution 26(4), 183–192 (2011) https://doi.org/10.1016/j.tree.2011.01.009 Siefert et al. [2015] Siefert, A., Violle, C., Chalmandrier, L., Albert, C.H., Taudiere, A., Fajardo, A., Aarssen, L.W., Baraloto, C., Carlucci, M.B., Cianciaruso, M.V., L. Dantas, V., Bello, F., Duarte, L.D.S., Fonseca, C.R., Freschet, G.T., Gaucherand, S., Gross, N., Hikosaka, K., Jackson, B., Jung, V., Kamiyama, C., Katabuchi, M., Kembel, S.W., Kichenin, E., Kraft, N.J.B., Lagerström, A., Bagousse-Pinguet, Y.L., Li, Y., Mason, N., Messier, J., Nakashizuka, T., Overton, J.M., Peltzer, D.A., Pérez-Ramos, I.M., Pillar, V.D., Prentice, H.C., Richardson, S., Sasaki, T., Schamp, B.S., Schöb, C., Shipley, B., Sundqvist, M., Sykes, M.T., Vandewalle, M., Wardle, D.A.: A global meta-analysis of the relative extent of intraspecific trait variation in plant communities. Ecology Letters 18(12), 1406–1419 (2015) https://doi.org/10.1111/ele.12508 Forsythe et al. 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[2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Johnson, N.F., Velásquez, N., Restrepo, N.J., Leahy, R., Gabriel, N., El Oud, S., Zheng, M., Manrique, P., Wuchty, S., Lupu, Y.: The online competition between pro-and anti-vaccination views. Nature 582(7811), 230–233 (2020) Illari et al. [2022] Illari, L., Restrepo, N.J., Johnson, N.F.: Losing the battle over best-science guidance early in a crisis: Covid-19 and beyond. Science Advances 8(39), 8017 (2022) https://doi.org/10.1126/sciadv.abo8017 Bolnick et al. [2011] Bolnick, D.I., Amarasekare, P., Araújo, M.S., Bürger, R., Levine, J.M., Novak, M., Rudolf, V.H.W., Schreiber, S.J., Urban, M.C., Vasseur, D.A.: Why intraspecific trait variation matters in community ecology. 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[2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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[2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Bolnick, D.I., Amarasekare, P., Araújo, M.S., Bürger, R., Levine, J.M., Novak, M., Rudolf, V.H.W., Schreiber, S.J., Urban, M.C., Vasseur, D.A.: Why intraspecific trait variation matters in community ecology. Trends in ecology & evolution 26(4), 183–192 (2011) https://doi.org/10.1016/j.tree.2011.01.009 Siefert et al. [2015] Siefert, A., Violle, C., Chalmandrier, L., Albert, C.H., Taudiere, A., Fajardo, A., Aarssen, L.W., Baraloto, C., Carlucci, M.B., Cianciaruso, M.V., L. Dantas, V., Bello, F., Duarte, L.D.S., Fonseca, C.R., Freschet, G.T., Gaucherand, S., Gross, N., Hikosaka, K., Jackson, B., Jung, V., Kamiyama, C., Katabuchi, M., Kembel, S.W., Kichenin, E., Kraft, N.J.B., Lagerström, A., Bagousse-Pinguet, Y.L., Li, Y., Mason, N., Messier, J., Nakashizuka, T., Overton, J.M., Peltzer, D.A., Pérez-Ramos, I.M., Pillar, V.D., Prentice, H.C., Richardson, S., Sasaki, T., Schamp, B.S., Schöb, C., Shipley, B., Sundqvist, M., Sykes, M.T., Vandewalle, M., Wardle, D.A.: A global meta-analysis of the relative extent of intraspecific trait variation in plant communities. Ecology Letters 18(12), 1406–1419 (2015) https://doi.org/10.1111/ele.12508 Forsythe et al. [2021] Forsythe, A.B., Day, T., Nelson, W.A.: Demystifying individual heterogeneity. Ecology Letters 24(10), 2282–2297 (2021) https://doi.org/10.1111/ele.13843 Jackson and Xue [2023] Jackson, Z., Xue, B.: Heterogeneity of interaction strengths and its consequences on ecological systems. Sci Rep 13(1905) (2023) https://doi.org/10.1038/s41598-023-28473-8 Johnson et al. [2016] Johnson, N.F., Zheng, M., Vorobyeva, Y., Gabriel, A., Qi, H., Velásquez, N., Manrique, P., Johnson, D., Restrepo, E., Song, C., et al.: New online ecology of adversarial aggregates: Isis and beyond. Science 352(6292), 1459–1463 (2016) Manrique et al. [2018] Manrique, P.D., Zheng, M., Cao, Z., Restrepo, E.M., Johnson, N.F.: Generalized gelation theory describes onset of online extremist support. Phys. Rev. Lett. 121(4), 048301 (2018) Velásquez et al. [2021] Velásquez, N., Manrique, P., Sear, R., et al.: Hidden order across online extremist movements can be disrupted by nudging collective chemistry. Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. [2023] Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. 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[2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Siefert, A., Violle, C., Chalmandrier, L., Albert, C.H., Taudiere, A., Fajardo, A., Aarssen, L.W., Baraloto, C., Carlucci, M.B., Cianciaruso, M.V., L. Dantas, V., Bello, F., Duarte, L.D.S., Fonseca, C.R., Freschet, G.T., Gaucherand, S., Gross, N., Hikosaka, K., Jackson, B., Jung, V., Kamiyama, C., Katabuchi, M., Kembel, S.W., Kichenin, E., Kraft, N.J.B., Lagerström, A., Bagousse-Pinguet, Y.L., Li, Y., Mason, N., Messier, J., Nakashizuka, T., Overton, J.M., Peltzer, D.A., Pérez-Ramos, I.M., Pillar, V.D., Prentice, H.C., Richardson, S., Sasaki, T., Schamp, B.S., Schöb, C., Shipley, B., Sundqvist, M., Sykes, M.T., Vandewalle, M., Wardle, D.A.: A global meta-analysis of the relative extent of intraspecific trait variation in plant communities. Ecology Letters 18(12), 1406–1419 (2015) https://doi.org/10.1111/ele.12508 Forsythe et al. [2021] Forsythe, A.B., Day, T., Nelson, W.A.: Demystifying individual heterogeneity. Ecology Letters 24(10), 2282–2297 (2021) https://doi.org/10.1111/ele.13843 Jackson and Xue [2023] Jackson, Z., Xue, B.: Heterogeneity of interaction strengths and its consequences on ecological systems. Sci Rep 13(1905) (2023) https://doi.org/10.1038/s41598-023-28473-8 Johnson et al. [2016] Johnson, N.F., Zheng, M., Vorobyeva, Y., Gabriel, A., Qi, H., Velásquez, N., Manrique, P., Johnson, D., Restrepo, E., Song, C., et al.: New online ecology of adversarial aggregates: Isis and beyond. Science 352(6292), 1459–1463 (2016) Manrique et al. [2018] Manrique, P.D., Zheng, M., Cao, Z., Restrepo, E.M., Johnson, N.F.: Generalized gelation theory describes onset of online extremist support. Phys. Rev. Lett. 121(4), 048301 (2018) Velásquez et al. [2021] Velásquez, N., Manrique, P., Sear, R., et al.: Hidden order across online extremist movements can be disrupted by nudging collective chemistry. Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. [2023] Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. Lett. 130, 237401 (2023) https://doi.org/10.1103/PhysRevLett.130.237401 Krapivsky et al. [2010] Krapivsky, P.L., Redner, S., Ben-Naim, E.: A Kinetic View of Statistical Physics. Cambridge University Press, ??? (2010). https://doi.org/10.1017/CBO9780511780516 Newman [2018] Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. [2009] Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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Science 352(6292), 1459–1463 (2016) Manrique et al. [2018] Manrique, P.D., Zheng, M., Cao, Z., Restrepo, E.M., Johnson, N.F.: Generalized gelation theory describes onset of online extremist support. Phys. Rev. Lett. 121(4), 048301 (2018) Velásquez et al. [2021] Velásquez, N., Manrique, P., Sear, R., et al.: Hidden order across online extremist movements can be disrupted by nudging collective chemistry. Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. [2023] Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. Lett. 130, 237401 (2023) https://doi.org/10.1103/PhysRevLett.130.237401 Krapivsky et al. [2010] Krapivsky, P.L., Redner, S., Ben-Naim, E.: A Kinetic View of Statistical Physics. Cambridge University Press, ??? (2010). https://doi.org/10.1017/CBO9780511780516 Newman [2018] Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. [2009] Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. 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[2009] Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. 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[2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Manrique, P.D., Zheng, M., Cao, Z., Restrepo, E.M., Johnson, N.F.: Generalized gelation theory describes onset of online extremist support. Phys. Rev. Lett. 121(4), 048301 (2018) Velásquez et al. [2021] Velásquez, N., Manrique, P., Sear, R., et al.: Hidden order across online extremist movements can be disrupted by nudging collective chemistry. Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. 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Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. 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[2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. [2009] Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. 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[2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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[2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. 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Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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[2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Lipiński, W.P., Visser, B.S., Robu, I., Fakhree, M.A.A., Lindhoud, S., Claessens, M.M.A.E., Spruijt, E.: Biomolecular condensates can both accelerate and suppress aggregation of α𝛼\alphaitalic_α-synuclein. Science Advances 8(48), 6495 (2022) https://doi.org/10.1126/sciadv.abq6495 Johnson et al. [2020] Johnson, N.F., Velásquez, N., Restrepo, N.J., Leahy, R., Gabriel, N., El Oud, S., Zheng, M., Manrique, P., Wuchty, S., Lupu, Y.: The online competition between pro-and anti-vaccination views. Nature 582(7811), 230–233 (2020) Illari et al. [2022] Illari, L., Restrepo, N.J., Johnson, N.F.: Losing the battle over best-science guidance early in a crisis: Covid-19 and beyond. Science Advances 8(39), 8017 (2022) https://doi.org/10.1126/sciadv.abo8017 Bolnick et al. [2011] Bolnick, D.I., Amarasekare, P., Araújo, M.S., Bürger, R., Levine, J.M., Novak, M., Rudolf, V.H.W., Schreiber, S.J., Urban, M.C., Vasseur, D.A.: Why intraspecific trait variation matters in community ecology. Trends in ecology & evolution 26(4), 183–192 (2011) https://doi.org/10.1016/j.tree.2011.01.009 Siefert et al. [2015] Siefert, A., Violle, C., Chalmandrier, L., Albert, C.H., Taudiere, A., Fajardo, A., Aarssen, L.W., Baraloto, C., Carlucci, M.B., Cianciaruso, M.V., L. Dantas, V., Bello, F., Duarte, L.D.S., Fonseca, C.R., Freschet, G.T., Gaucherand, S., Gross, N., Hikosaka, K., Jackson, B., Jung, V., Kamiyama, C., Katabuchi, M., Kembel, S.W., Kichenin, E., Kraft, N.J.B., Lagerström, A., Bagousse-Pinguet, Y.L., Li, Y., Mason, N., Messier, J., Nakashizuka, T., Overton, J.M., Peltzer, D.A., Pérez-Ramos, I.M., Pillar, V.D., Prentice, H.C., Richardson, S., Sasaki, T., Schamp, B.S., Schöb, C., Shipley, B., Sundqvist, M., Sykes, M.T., Vandewalle, M., Wardle, D.A.: A global meta-analysis of the relative extent of intraspecific trait variation in plant communities. Ecology Letters 18(12), 1406–1419 (2015) https://doi.org/10.1111/ele.12508 Forsythe et al. [2021] Forsythe, A.B., Day, T., Nelson, W.A.: Demystifying individual heterogeneity. Ecology Letters 24(10), 2282–2297 (2021) https://doi.org/10.1111/ele.13843 Jackson and Xue [2023] Jackson, Z., Xue, B.: Heterogeneity of interaction strengths and its consequences on ecological systems. 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[2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. 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[2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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[2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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[2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. 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Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. 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[2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Lipiński, W.P., Visser, B.S., Robu, I., Fakhree, M.A.A., Lindhoud, S., Claessens, M.M.A.E., Spruijt, E.: Biomolecular condensates can both accelerate and suppress aggregation of α𝛼\alphaitalic_α-synuclein. Science Advances 8(48), 6495 (2022) https://doi.org/10.1126/sciadv.abq6495 Johnson et al. [2020] Johnson, N.F., Velásquez, N., Restrepo, N.J., Leahy, R., Gabriel, N., El Oud, S., Zheng, M., Manrique, P., Wuchty, S., Lupu, Y.: The online competition between pro-and anti-vaccination views. Nature 582(7811), 230–233 (2020) Illari et al. [2022] Illari, L., Restrepo, N.J., Johnson, N.F.: Losing the battle over best-science guidance early in a crisis: Covid-19 and beyond. 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Dantas, V., Bello, F., Duarte, L.D.S., Fonseca, C.R., Freschet, G.T., Gaucherand, S., Gross, N., Hikosaka, K., Jackson, B., Jung, V., Kamiyama, C., Katabuchi, M., Kembel, S.W., Kichenin, E., Kraft, N.J.B., Lagerström, A., Bagousse-Pinguet, Y.L., Li, Y., Mason, N., Messier, J., Nakashizuka, T., Overton, J.M., Peltzer, D.A., Pérez-Ramos, I.M., Pillar, V.D., Prentice, H.C., Richardson, S., Sasaki, T., Schamp, B.S., Schöb, C., Shipley, B., Sundqvist, M., Sykes, M.T., Vandewalle, M., Wardle, D.A.: A global meta-analysis of the relative extent of intraspecific trait variation in plant communities. Ecology Letters 18(12), 1406–1419 (2015) https://doi.org/10.1111/ele.12508 Forsythe et al. [2021] Forsythe, A.B., Day, T., Nelson, W.A.: Demystifying individual heterogeneity. Ecology Letters 24(10), 2282–2297 (2021) https://doi.org/10.1111/ele.13843 Jackson and Xue [2023] Jackson, Z., Xue, B.: Heterogeneity of interaction strengths and its consequences on ecological systems. 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[2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Johnson, N.F., Velásquez, N., Restrepo, N.J., Leahy, R., Gabriel, N., El Oud, S., Zheng, M., Manrique, P., Wuchty, S., Lupu, Y.: The online competition between pro-and anti-vaccination views. Nature 582(7811), 230–233 (2020) Illari et al. [2022] Illari, L., Restrepo, N.J., Johnson, N.F.: Losing the battle over best-science guidance early in a crisis: Covid-19 and beyond. Science Advances 8(39), 8017 (2022) https://doi.org/10.1126/sciadv.abo8017 Bolnick et al. [2011] Bolnick, D.I., Amarasekare, P., Araújo, M.S., Bürger, R., Levine, J.M., Novak, M., Rudolf, V.H.W., Schreiber, S.J., Urban, M.C., Vasseur, D.A.: Why intraspecific trait variation matters in community ecology. 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Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Bolnick, D.I., Amarasekare, P., Araújo, M.S., Bürger, R., Levine, J.M., Novak, M., Rudolf, V.H.W., Schreiber, S.J., Urban, M.C., Vasseur, D.A.: Why intraspecific trait variation matters in community ecology. Trends in ecology & evolution 26(4), 183–192 (2011) https://doi.org/10.1016/j.tree.2011.01.009 Siefert et al. [2015] Siefert, A., Violle, C., Chalmandrier, L., Albert, C.H., Taudiere, A., Fajardo, A., Aarssen, L.W., Baraloto, C., Carlucci, M.B., Cianciaruso, M.V., L. Dantas, V., Bello, F., Duarte, L.D.S., Fonseca, C.R., Freschet, G.T., Gaucherand, S., Gross, N., Hikosaka, K., Jackson, B., Jung, V., Kamiyama, C., Katabuchi, M., Kembel, S.W., Kichenin, E., Kraft, N.J.B., Lagerström, A., Bagousse-Pinguet, Y.L., Li, Y., Mason, N., Messier, J., Nakashizuka, T., Overton, J.M., Peltzer, D.A., Pérez-Ramos, I.M., Pillar, V.D., Prentice, H.C., Richardson, S., Sasaki, T., Schamp, B.S., Schöb, C., Shipley, B., Sundqvist, M., Sykes, M.T., Vandewalle, M., Wardle, D.A.: A global meta-analysis of the relative extent of intraspecific trait variation in plant communities. Ecology Letters 18(12), 1406–1419 (2015) https://doi.org/10.1111/ele.12508 Forsythe et al. [2021] Forsythe, A.B., Day, T., Nelson, W.A.: Demystifying individual heterogeneity. Ecology Letters 24(10), 2282–2297 (2021) https://doi.org/10.1111/ele.13843 Jackson and Xue [2023] Jackson, Z., Xue, B.: Heterogeneity of interaction strengths and its consequences on ecological systems. Sci Rep 13(1905) (2023) https://doi.org/10.1038/s41598-023-28473-8 Johnson et al. [2016] Johnson, N.F., Zheng, M., Vorobyeva, Y., Gabriel, A., Qi, H., Velásquez, N., Manrique, P., Johnson, D., Restrepo, E., Song, C., et al.: New online ecology of adversarial aggregates: Isis and beyond. Science 352(6292), 1459–1463 (2016) Manrique et al. [2018] Manrique, P.D., Zheng, M., Cao, Z., Restrepo, E.M., Johnson, N.F.: Generalized gelation theory describes onset of online extremist support. Phys. Rev. Lett. 121(4), 048301 (2018) Velásquez et al. [2021] Velásquez, N., Manrique, P., Sear, R., et al.: Hidden order across online extremist movements can be disrupted by nudging collective chemistry. Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. [2023] Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. Lett. 130, 237401 (2023) https://doi.org/10.1103/PhysRevLett.130.237401 Krapivsky et al. [2010] Krapivsky, P.L., Redner, S., Ben-Naim, E.: A Kinetic View of Statistical Physics. Cambridge University Press, ??? (2010). https://doi.org/10.1017/CBO9780511780516 Newman [2018] Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. [2009] Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. 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[2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Velásquez, N., Manrique, P., Sear, R., et al.: Hidden order across online extremist movements can be disrupted by nudging collective chemistry. Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. [2023] Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. Lett. 130, 237401 (2023) https://doi.org/10.1103/PhysRevLett.130.237401 Krapivsky et al. [2010] Krapivsky, P.L., Redner, S., Ben-Naim, E.: A Kinetic View of Statistical Physics. Cambridge University Press, ??? (2010). https://doi.org/10.1017/CBO9780511780516 Newman [2018] Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. [2009] Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. 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[2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. Lett. 130, 237401 (2023) https://doi.org/10.1103/PhysRevLett.130.237401 Krapivsky et al. [2010] Krapivsky, P.L., Redner, S., Ben-Naim, E.: A Kinetic View of Statistical Physics. Cambridge University Press, ??? (2010). https://doi.org/10.1017/CBO9780511780516 Newman [2018] Newman, M.: Networks. 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Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. 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[2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. 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Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. 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Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. 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[2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. 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[2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. 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Dantas, V., Bello, F., Duarte, L.D.S., Fonseca, C.R., Freschet, G.T., Gaucherand, S., Gross, N., Hikosaka, K., Jackson, B., Jung, V., Kamiyama, C., Katabuchi, M., Kembel, S.W., Kichenin, E., Kraft, N.J.B., Lagerström, A., Bagousse-Pinguet, Y.L., Li, Y., Mason, N., Messier, J., Nakashizuka, T., Overton, J.M., Peltzer, D.A., Pérez-Ramos, I.M., Pillar, V.D., Prentice, H.C., Richardson, S., Sasaki, T., Schamp, B.S., Schöb, C., Shipley, B., Sundqvist, M., Sykes, M.T., Vandewalle, M., Wardle, D.A.: A global meta-analysis of the relative extent of intraspecific trait variation in plant communities. Ecology Letters 18(12), 1406–1419 (2015) https://doi.org/10.1111/ele.12508 Forsythe et al. [2021] Forsythe, A.B., Day, T., Nelson, W.A.: Demystifying individual heterogeneity. Ecology Letters 24(10), 2282–2297 (2021) https://doi.org/10.1111/ele.13843 Jackson and Xue [2023] Jackson, Z., Xue, B.: Heterogeneity of interaction strengths and its consequences on ecological systems. 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E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Forsythe, A.B., Day, T., Nelson, W.A.: Demystifying individual heterogeneity. Ecology Letters 24(10), 2282–2297 (2021) https://doi.org/10.1111/ele.13843 Jackson and Xue [2023] Jackson, Z., Xue, B.: Heterogeneity of interaction strengths and its consequences on ecological systems. Sci Rep 13(1905) (2023) https://doi.org/10.1038/s41598-023-28473-8 Johnson et al. [2016] Johnson, N.F., Zheng, M., Vorobyeva, Y., Gabriel, A., Qi, H., Velásquez, N., Manrique, P., Johnson, D., Restrepo, E., Song, C., et al.: New online ecology of adversarial aggregates: Isis and beyond. Science 352(6292), 1459–1463 (2016) Manrique et al. 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Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. 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[2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Manrique, P.D., Zheng, M., Cao, Z., Restrepo, E.M., Johnson, N.F.: Generalized gelation theory describes onset of online extremist support. Phys. Rev. Lett. 121(4), 048301 (2018) Velásquez et al. [2021] Velásquez, N., Manrique, P., Sear, R., et al.: Hidden order across online extremist movements can be disrupted by nudging collective chemistry. Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. 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Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. 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Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. 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[2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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[2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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[2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. 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Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Siefert, A., Violle, C., Chalmandrier, L., Albert, C.H., Taudiere, A., Fajardo, A., Aarssen, L.W., Baraloto, C., Carlucci, M.B., Cianciaruso, M.V., L. Dantas, V., Bello, F., Duarte, L.D.S., Fonseca, C.R., Freschet, G.T., Gaucherand, S., Gross, N., Hikosaka, K., Jackson, B., Jung, V., Kamiyama, C., Katabuchi, M., Kembel, S.W., Kichenin, E., Kraft, N.J.B., Lagerström, A., Bagousse-Pinguet, Y.L., Li, Y., Mason, N., Messier, J., Nakashizuka, T., Overton, J.M., Peltzer, D.A., Pérez-Ramos, I.M., Pillar, V.D., Prentice, H.C., Richardson, S., Sasaki, T., Schamp, B.S., Schöb, C., Shipley, B., Sundqvist, M., Sykes, M.T., Vandewalle, M., Wardle, D.A.: A global meta-analysis of the relative extent of intraspecific trait variation in plant communities. Ecology Letters 18(12), 1406–1419 (2015) https://doi.org/10.1111/ele.12508 Forsythe et al. [2021] Forsythe, A.B., Day, T., Nelson, W.A.: Demystifying individual heterogeneity. Ecology Letters 24(10), 2282–2297 (2021) https://doi.org/10.1111/ele.13843 Jackson and Xue [2023] Jackson, Z., Xue, B.: Heterogeneity of interaction strengths and its consequences on ecological systems. Sci Rep 13(1905) (2023) https://doi.org/10.1038/s41598-023-28473-8 Johnson et al. [2016] Johnson, N.F., Zheng, M., Vorobyeva, Y., Gabriel, A., Qi, H., Velásquez, N., Manrique, P., Johnson, D., Restrepo, E., Song, C., et al.: New online ecology of adversarial aggregates: Isis and beyond. Science 352(6292), 1459–1463 (2016) Manrique et al. [2018] Manrique, P.D., Zheng, M., Cao, Z., Restrepo, E.M., Johnson, N.F.: Generalized gelation theory describes onset of online extremist support. Phys. Rev. Lett. 121(4), 048301 (2018) Velásquez et al. [2021] Velásquez, N., Manrique, P., Sear, R., et al.: Hidden order across online extremist movements can be disrupted by nudging collective chemistry. Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. [2023] Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. 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Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Forsythe, A.B., Day, T., Nelson, W.A.: Demystifying individual heterogeneity. Ecology Letters 24(10), 2282–2297 (2021) https://doi.org/10.1111/ele.13843 Jackson and Xue [2023] Jackson, Z., Xue, B.: Heterogeneity of interaction strengths and its consequences on ecological systems. Sci Rep 13(1905) (2023) https://doi.org/10.1038/s41598-023-28473-8 Johnson et al. [2016] Johnson, N.F., Zheng, M., Vorobyeva, Y., Gabriel, A., Qi, H., Velásquez, N., Manrique, P., Johnson, D., Restrepo, E., Song, C., et al.: New online ecology of adversarial aggregates: Isis and beyond. Science 352(6292), 1459–1463 (2016) Manrique et al. 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Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. 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[2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. 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Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. 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[2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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[2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. 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E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Illari, L., Restrepo, N.J., Johnson, N.F.: Losing the battle over best-science guidance early in a crisis: Covid-19 and beyond. Science Advances 8(39), 8017 (2022) https://doi.org/10.1126/sciadv.abo8017 Bolnick et al. [2011] Bolnick, D.I., Amarasekare, P., Araújo, M.S., Bürger, R., Levine, J.M., Novak, M., Rudolf, V.H.W., Schreiber, S.J., Urban, M.C., Vasseur, D.A.: Why intraspecific trait variation matters in community ecology. Trends in ecology & evolution 26(4), 183–192 (2011) https://doi.org/10.1016/j.tree.2011.01.009 Siefert et al. [2015] Siefert, A., Violle, C., Chalmandrier, L., Albert, C.H., Taudiere, A., Fajardo, A., Aarssen, L.W., Baraloto, C., Carlucci, M.B., Cianciaruso, M.V., L. 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[2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Bolnick, D.I., Amarasekare, P., Araújo, M.S., Bürger, R., Levine, J.M., Novak, M., Rudolf, V.H.W., Schreiber, S.J., Urban, M.C., Vasseur, D.A.: Why intraspecific trait variation matters in community ecology. Trends in ecology & evolution 26(4), 183–192 (2011) https://doi.org/10.1016/j.tree.2011.01.009 Siefert et al. [2015] Siefert, A., Violle, C., Chalmandrier, L., Albert, C.H., Taudiere, A., Fajardo, A., Aarssen, L.W., Baraloto, C., Carlucci, M.B., Cianciaruso, M.V., L. Dantas, V., Bello, F., Duarte, L.D.S., Fonseca, C.R., Freschet, G.T., Gaucherand, S., Gross, N., Hikosaka, K., Jackson, B., Jung, V., Kamiyama, C., Katabuchi, M., Kembel, S.W., Kichenin, E., Kraft, N.J.B., Lagerström, A., Bagousse-Pinguet, Y.L., Li, Y., Mason, N., Messier, J., Nakashizuka, T., Overton, J.M., Peltzer, D.A., Pérez-Ramos, I.M., Pillar, V.D., Prentice, H.C., Richardson, S., Sasaki, T., Schamp, B.S., Schöb, C., Shipley, B., Sundqvist, M., Sykes, M.T., Vandewalle, M., Wardle, D.A.: A global meta-analysis of the relative extent of intraspecific trait variation in plant communities. Ecology Letters 18(12), 1406–1419 (2015) https://doi.org/10.1111/ele.12508 Forsythe et al. [2021] Forsythe, A.B., Day, T., Nelson, W.A.: Demystifying individual heterogeneity. Ecology Letters 24(10), 2282–2297 (2021) https://doi.org/10.1111/ele.13843 Jackson and Xue [2023] Jackson, Z., Xue, B.: Heterogeneity of interaction strengths and its consequences on ecological systems. 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[2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Velásquez, N., Manrique, P., Sear, R., et al.: Hidden order across online extremist movements can be disrupted by nudging collective chemistry. Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. [2023] Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. Lett. 130, 237401 (2023) https://doi.org/10.1103/PhysRevLett.130.237401 Krapivsky et al. [2010] Krapivsky, P.L., Redner, S., Ben-Naim, E.: A Kinetic View of Statistical Physics. Cambridge University Press, ??? (2010). https://doi.org/10.1017/CBO9780511780516 Newman [2018] Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. 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[2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. 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[2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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[2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. 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Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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Dantas, V., Bello, F., Duarte, L.D.S., Fonseca, C.R., Freschet, G.T., Gaucherand, S., Gross, N., Hikosaka, K., Jackson, B., Jung, V., Kamiyama, C., Katabuchi, M., Kembel, S.W., Kichenin, E., Kraft, N.J.B., Lagerström, A., Bagousse-Pinguet, Y.L., Li, Y., Mason, N., Messier, J., Nakashizuka, T., Overton, J.M., Peltzer, D.A., Pérez-Ramos, I.M., Pillar, V.D., Prentice, H.C., Richardson, S., Sasaki, T., Schamp, B.S., Schöb, C., Shipley, B., Sundqvist, M., Sykes, M.T., Vandewalle, M., Wardle, D.A.: A global meta-analysis of the relative extent of intraspecific trait variation in plant communities. Ecology Letters 18(12), 1406–1419 (2015) https://doi.org/10.1111/ele.12508 Forsythe et al. [2021] Forsythe, A.B., Day, T., Nelson, W.A.: Demystifying individual heterogeneity. Ecology Letters 24(10), 2282–2297 (2021) https://doi.org/10.1111/ele.13843 Jackson and Xue [2023] Jackson, Z., Xue, B.: Heterogeneity of interaction strengths and its consequences on ecological systems. 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E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Forsythe, A.B., Day, T., Nelson, W.A.: Demystifying individual heterogeneity. Ecology Letters 24(10), 2282–2297 (2021) https://doi.org/10.1111/ele.13843 Jackson and Xue [2023] Jackson, Z., Xue, B.: Heterogeneity of interaction strengths and its consequences on ecological systems. Sci Rep 13(1905) (2023) https://doi.org/10.1038/s41598-023-28473-8 Johnson et al. [2016] Johnson, N.F., Zheng, M., Vorobyeva, Y., Gabriel, A., Qi, H., Velásquez, N., Manrique, P., Johnson, D., Restrepo, E., Song, C., et al.: New online ecology of adversarial aggregates: Isis and beyond. Science 352(6292), 1459–1463 (2016) Manrique et al. [2018] Manrique, P.D., Zheng, M., Cao, Z., Restrepo, E.M., Johnson, N.F.: Generalized gelation theory describes onset of online extremist support. Phys. Rev. Lett. 121(4), 048301 (2018) Velásquez et al. [2021] Velásquez, N., Manrique, P., Sear, R., et al.: Hidden order across online extremist movements can be disrupted by nudging collective chemistry. Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. [2023] Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. Lett. 130, 237401 (2023) https://doi.org/10.1103/PhysRevLett.130.237401 Krapivsky et al. [2010] Krapivsky, P.L., Redner, S., Ben-Naim, E.: A Kinetic View of Statistical Physics. Cambridge University Press, ??? (2010). https://doi.org/10.1017/CBO9780511780516 Newman [2018] Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. 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Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. 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Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. 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[2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. 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[2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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[2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. 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[2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. 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Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. 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[2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. 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[2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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[2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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[2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. 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Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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Science 352(6292), 1459–1463 (2016) Manrique et al. [2018] Manrique, P.D., Zheng, M., Cao, Z., Restrepo, E.M., Johnson, N.F.: Generalized gelation theory describes onset of online extremist support. Phys. Rev. Lett. 121(4), 048301 (2018) Velásquez et al. [2021] Velásquez, N., Manrique, P., Sear, R., et al.: Hidden order across online extremist movements can be disrupted by nudging collective chemistry. Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. [2023] Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. Lett. 130, 237401 (2023) https://doi.org/10.1103/PhysRevLett.130.237401 Krapivsky et al. [2010] Krapivsky, P.L., Redner, S., Ben-Naim, E.: A Kinetic View of Statistical Physics. Cambridge University Press, ??? (2010). https://doi.org/10.1017/CBO9780511780516 Newman [2018] Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. [2009] Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. 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[2009] Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. 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E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Velásquez, N., Manrique, P., Sear, R., et al.: Hidden order across online extremist movements can be disrupted by nudging collective chemistry. Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. [2023] Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. Lett. 130, 237401 (2023) https://doi.org/10.1103/PhysRevLett.130.237401 Krapivsky et al. [2010] Krapivsky, P.L., Redner, S., Ben-Naim, E.: A Kinetic View of Statistical Physics. Cambridge University Press, ??? (2010). https://doi.org/10.1017/CBO9780511780516 Newman [2018] Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. 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Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. 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Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. 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[2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Krapivsky, P.L., Redner, S., Ben-Naim, E.: A Kinetic View of Statistical Physics. Cambridge University Press, ??? (2010). https://doi.org/10.1017/CBO9780511780516 Newman [2018] Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. [2009] Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. 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[2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. 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CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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[2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. 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CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. 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[2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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[2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Velásquez, N., Manrique, P., Sear, R., et al.: Hidden order across online extremist movements can be disrupted by nudging collective chemistry. Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. [2023] Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. Lett. 130, 237401 (2023) https://doi.org/10.1103/PhysRevLett.130.237401 Krapivsky et al. [2010] Krapivsky, P.L., Redner, S., Ben-Naim, E.: A Kinetic View of Statistical Physics. Cambridge University Press, ??? (2010). https://doi.org/10.1017/CBO9780511780516 Newman [2018] Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. 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Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. 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Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. 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[2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. 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Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. 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Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. 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[2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. 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[2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. 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Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Velásquez, N., Manrique, P., Sear, R., et al.: Hidden order across online extremist movements can be disrupted by nudging collective chemistry. Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. [2023] Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. Lett. 130, 237401 (2023) https://doi.org/10.1103/PhysRevLett.130.237401 Krapivsky et al. [2010] Krapivsky, P.L., Redner, S., Ben-Naim, E.: A Kinetic View of Statistical Physics. Cambridge University Press, ??? (2010). https://doi.org/10.1017/CBO9780511780516 Newman [2018] Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. 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Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. 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[2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Krapivsky, P.L., Redner, S., Ben-Naim, E.: A Kinetic View of Statistical Physics. Cambridge University Press, ??? (2010). https://doi.org/10.1017/CBO9780511780516 Newman [2018] Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. [2009] Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. 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Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. 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[2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. 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[2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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[2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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[2023] Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. Lett. 130, 237401 (2023) https://doi.org/10.1103/PhysRevLett.130.237401 Krapivsky et al. [2010] Krapivsky, P.L., Redner, S., Ben-Naim, E.: A Kinetic View of Statistical Physics. Cambridge University Press, ??? (2010). https://doi.org/10.1017/CBO9780511780516 Newman [2018] Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. [2009] Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Manrique, P.D., Zheng, M., Cao, Z., Restrepo, E.M., Johnson, N.F.: Generalized gelation theory describes onset of online extremist support. Phys. Rev. Lett. 121(4), 048301 (2018) Velásquez et al. [2021] Velásquez, N., Manrique, P., Sear, R., et al.: Hidden order across online extremist movements can be disrupted by nudging collective chemistry. Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. [2023] Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. Lett. 130, 237401 (2023) https://doi.org/10.1103/PhysRevLett.130.237401 Krapivsky et al. 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Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. 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Sci. Rep. 11(9965) (2021) https://doi.org/10.1038/s41598-021-89349-3 Manrique et al. [2023] Manrique, P.D., Huo, F.Y., El Oud, S., Zheng, M., Illari, L., Johnson, N.F.: Shockwavelike behavior across social media. Phys. Rev. Lett. 130, 237401 (2023) https://doi.org/10.1103/PhysRevLett.130.237401 Krapivsky et al. [2010] Krapivsky, P.L., Redner, S., Ben-Naim, E.: A Kinetic View of Statistical Physics. Cambridge University Press, ??? (2010). https://doi.org/10.1017/CBO9780511780516 Newman [2018] Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. [2009] Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. 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Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. 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E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. 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[2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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[2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. 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Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. 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[2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. 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[2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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[2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. 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Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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[2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. 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CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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[2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. 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CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. 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[2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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[2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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[2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Newman, M.: Networks. Oxford University Press, Oxford, UK (2018) Maji et al. [2009] Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Maji, S.K., Perrin, M.H., Sawaya, M.R., Jessberger, S., Vadodaria, K., Rissman, R.A., Singru, P.S., Nilsson, K.P.R., Simon, R., Schubert, D., Eisenberg, D., Rivier, J., Sawchenko, P., Vale, W., Riek, R.: Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325(5938), 328–332 (2009) https://doi.org/10.1126/science.1173155 Knowles and Buehler [2011] Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Knowles, T., Buehler, M.: Nanomechanics of functional and pathological amyloid materials. Nature Nanotech. 6, 469–479 (2011) https://doi.org/10.1038/nnano.2011.102 Knowles and Mezzenga [2016] Knowles, T.P.J., Mezzenga, R.: Amyloid fibrils as building blocks for natural and artificial functional materials. Advanced Materials 28(31), 6546–6561 (2016) https://doi.org/10.1002/adma.201505961 Soto and Pritzkow [2018] Soto, C., Pritzkow, S.: Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases. Nat. Neurosci. 21, 1332–1340 (2018) https://doi.org/10.1038/s41593-018-0235-9 Hipp et al. [2019] Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. 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[2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. 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[2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. 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[2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. 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[2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Hipp, M.S., Kasturi, P., Hartl, F.U.: The proteostasis network and its decline in ageing. Nat Rev Mol Cell Biol 20, 421–435 (2019) https://doi.org/10.1038/s41580-019-0101-y Vendruscolo and Fuxreiter [2022] Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Vendruscolo, M., Fuxreiter, M.: Protein condensation diseases: therapeutic opportunities. Nat Commun 13(5550) (2022) https://doi.org/10.1038/s41467-022-32940-7 Chen and et al. [2017] Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. 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[2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Chen, G.-F., al.: “amyloid beta: structure, biology and structure-based therapeutic development.”. Acta pharmacologica Sinica 38(9), 1205–1235 (2017) https://doi.org/10.1038/aps.2017.28 Irwin et al. [2013] Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. 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[2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Irwin, D., Lee, V., Trojanowski, J.: Parkinson’s disease dementia: convergence of α𝛼\alphaitalic_α-synuclein, tau and amyloid-β𝛽\betaitalic_β pathologies. Nat. Rev. Neurosci. 14, 626–636 (2013) https://doi.org/10.1038/nrn3549 Ashraf [2014] Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Ashraf, G.M.e.a.: Protein misfolding and aggregation in alzheimer’s disease and type 2 diabetes mellitus. CNS & neurological disorders drug targets 13(7), 1280–1293 (2014) https://doi.org/10.2174/1871527313666140917095514 Butler [2003] Butler, A.E.e.a.: Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52(9), 2304–2314 (2003) https://doi.org/10.2337/diabetes.52.9.2304 Michaels et al. [2023] Michaels, T.C.T., Qian, D., al.: Amyloid formation as a protein phase transition. Nat. Rev. Phys. 5, 379–397 (2023) https://doi.org/10.1038/s42254-023-00598-9 Meisl et al. [2016] Meisl, G., Kirkegaard, J., Arosio, P.e.a.: Molecular mechanisms of protein aggregation from global fitting of kinetic models. Nat Protoc 11, 252–272 (2016) https://doi.org/10.1038/nprot.2016.010 Sinnige [2022] Sinnige, T.: Molecular mechanisms of amyloid formation in living systems. Chem. Sci. 13, 7080–7097 (2022) https://doi.org/10.1039/D2SC01278B Wang et al. [2021] Wang, B., Zhang, L., Dai, T.e.a.: Liquid–liquid phase separation in human health and diseases. Sig Transduct Target Ther 6(290) (2021) https://doi.org/10.1038/s41392-021-00678-1 Banani et al. [2017] Banani, S., Lee, H., Hyman, A.e.a.: Biomolecular condensates: organizers of cellular biochemistry. Nat Rev Mol Cell Biol 18, 285–298 (2017) https://doi.org/10.1038/nrm.2017.7 Sabari [2020] Sabari, B.R.: Biomolecular condensates and gene activation in development and disease. Developmental Cell 55(1), 84–96 (2020) https://doi.org/10.1016/j.devcel.2020.09.005 Nakashima et al. [2019] Nakashima, K.K., Vibhute, M.A., Spruijt, E.: Biomolecular chemistry in liquid phase separated compartments. Frontiers in Molecular Biosciences 6 (2019) https://doi.org/10.3389/fmolb.2019.00021 Weber et al. [2019] Weber, C., Michaels, T., Mahadevan, L.: Spatial control of irreversible protein aggregation. eLife 8, 42315 (2019) https://doi.org/10.7554/eLife.42315 Jamieson [2023] Jamieson, K.H.: Vaccine Confidence Falls as Belief in Health Misinformation Grows. University of Pennsylvania. Annenberg Public Policy Center (2023). https://www.annenbergpublicpolicycenter.org/vaccine-confidence-falls-as-belief-in-health-misinformation-grows/ Monte [2021] Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. 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- Monte, L.M.: Household Pulse Survey Shows Many Don’t Trust COVID Vaccine, Worry About Side Effects. U.S. Census Bureau (2021). https://www.census.gov/library/stories/2021/12/who-are-the-adults-not-vaccinated-against-covid.html Kemp [2022] Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311
- Kemp, S.: Digital 2022: October Global Statshot Report (2022). https://datareportal.com/reports/digital-2022-october-global-statshot Johnson et al. [2013] Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311
- Johnson, N.F., Manrique, P., Hui, P.M.: Modeling insurgent dynamics including heterogeneity. J. Stat. Phys. 151, 395–413 (2013) Manrique et al. [2015] Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311
- Manrique, P.D., Hui, P.M., Johnson, N.F.: Internal character dictates transition dynamics between isolation and cohesive grouping. Phys. Rev. E 92, 062803 (2015) https://doi.org/10.1103/PhysRevE.92.062803 Manrique and Johnson [2018] Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311 Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311
- Manrique, P.D., Johnson, N.F.: Individual heterogeneity generating explosive system network dynamics. Phys. Rev. E 97, 032311 (2018) https://doi.org/10.1103/PhysRevE.97.032311
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